supported by grants from the Norwegian University of Life Sciences and The Research Council of Norway(227386/E40).
The cellular prion protein PrPC has been extensively studied because it can adopt a pathogenic three-dimensional conformation that causes rare,but invariably fatal,neurodegenerative prion diseases in humans and other ...
Project supported by the Key Program of the National Key Research and Development Program of China (Grant No. 2016YFA0501702);the National Natural Science Foundation of China (Grant No. 11674065)。
Prion diseases are associated with the misfolding of the normal helical cellular form of prion protein (PrPC) into the β-sheet-rich scrapie form (PrPSc) and the subsequent aggregation of PrPSc into amyloid fibrils. R...
Supported by Alberta Prion Research Institute,Canada(Project title:"Comprehensive Risk Assessment of CWD Transmission to Humans Using Non-human Primates");European Metrology Research Programme(EMRP);Researcher Grant:HLT10-Bi Origin(Metrology for the Biomolecular Origin of Disease)
Proteinaceous infectious particles(prions) are unique pathogens as they are devoid of any coding nucleic acid.Whilst it is assumed that prion disease is transmitted by a misfolded isoform of the cellular prion protein...
This work was supported by National Natural Science Foundation of China 30070038 and 30130070, National High-Tech Research and Development Program of China (863 Project) 2001AA215391, and EU Project QLRT 2000 01441.
Objective To report a protocol using biotin-labelled PrP protein in cell free conversion assay instead of isotope. Methods A hamster PrP protein (HaPrP) was expressed in E. coli and purified with HIS-tag affinity ch...